Enzymatic properties of stingray Dasyatis pastinaca group V, IIA and IB phospholipases A2: A comparative study

Bacha, Abir Ben; Abid, Islem; Horchani, Habib; Mejdoub, Hafedh

doi:10.1016/j.ijbiomac.2013.10.003

Cited by 9 publications

(7 citation statements)

References 35 publications

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“…Notably, we have not detected the presence of contigs in P. motoro with high similarities to phospholipase A2, previously described in other members of the genus, as well as in the common stingray Dasyatis pastinaca , and in envenomation scenarios causing symptoms such as hemorrhage and necrosis [37].…”

Section: Resultsmentioning

confidence: 68%

Transcriptomic Characterization of the South American Freshwater Stingray Potamotrygon motoro Venom Apparatus

Silva

Huang

Yang

et al. 2018

Toxins

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Venomous animals are found through a wide taxonomic range including cartilaginous fish such as the freshwater stingray Potamotrygon motoro occurring in South America, which can injure people and cause venom-related symptoms. Ensuring the efficacy of drug development to treat stingray injuries can be assisted by the knowledge of the venom composition. Here we performed a detailed transcriptomic characterization of the venom gland of the South American freshwater stingray Potamotrygon motoro. The transcripts retrieved showed 418 hits to venom components (comparably to 426 and 396 hits in other two Potamotrygon species), with high expression levels of hyaluronidase, cystatin and calglandulin along with hits uniquely found in P. motoro such as DELTA-alicitoxin-Pse1b, Augerpeptide hhe53 and PI-actitoxin-Aeq3a. We also identified undescribed molecules with extremely high expression values with sequence similarity to the SE-cephalotoxin and Rapunzel genes. Comparative analyses showed that despite being closely related, there may be significant variation among the venoms of freshwater stingrays, highlighting the importance of considering elicit care in handling different envenomation cases. Since hyaluronidase represents a major component of fish venom, we have performed phylogenetic and selective pressure analyses of this gene/protein across all fish with the available information. Results indicated an independent recruitment of the hyaluronidase into the stingray venom relative to that of venomous bony fish. The hyaluronidase residues were found to be mostly under negative selection, but 18 sites showed evidence of diversifying positive selection (P < 0.05). Our data provides new insight into stingray venom variation, composition, and selective pressure in hyaluronidase.

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Section: Resultsmentioning

confidence: 68%

Transcriptomic Characterization of the South American Freshwater Stingray Potamotrygon motoro Venom Apparatus

Silva

Huang

Yang

et al. 2018

Toxins

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“…Whereas, phosphatidylserine (PS) showed the lowest specific activity with a specific activity of 32 U/mg ± 1.2. This observation is confirmed by the activity of group V PLA 2 from stingrays which hydrolyze PE (72 U/mg ± 1.5) and PC (52 U/mg ± 3.5) substrate more efficiently than PS substrate (18 U/mg ± 0.7) [ 35 ]. Besides, human heart sPLA2-V preferentially hydrolyzes PE vesicles compared to PC vesicles [ 36 ].…”

Section: Resultsmentioning

confidence: 76%

Biochemical, Kinetic and Biological Properties of Group V Phospholipase A2 from Dromedary

et al. 2022

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Secretory group V phospholipase A2 (PLA2-V) is known to be involved in inflammatory processes in cellular studies, nevertheless, the biochemical and the enzymatic characteristics of this important enzyme have been unclear yet. We reported, as a first step towards understanding the biochemical properties, catalytic characteristics, antimicrobial and cytotoxic effects of this PLA2, the production of PLA2-V from dromedary. The obtained DrPLA2-V has an absolute requirement for Ca2+ and NaTDC for enzymatic activity with an optimum pH of 9 and temperature of 45 °C with phosphatidylethanolamine as a substrate. Kinetic parameters showed that Kcat/Kmapp is 2.6 ± 0.02 mM−1 s−1. The enzyme was found to display potent Gram-positive bactericidal activity (with IC50 values of about 5 µg/mL) and antifungal activity (with IC50 values of about 25 µg/mL)in vitro. However, the purified enzyme did not display a cytotoxic effect against cancer cells.

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“…They have a vast spectrum of activities, such as neurotoxic, myotoxic, hemolytic, edematogenic, hyperalgesic, pro-inflammatory, hypotensive, platelet-aggregation inhibition, anticoagulant and cytotoxic, being one the most dangerous toxins in animals 31 . These enzymes have already been described in stingray venom from Dasyatis pastinaca 32 . Like metalloproteinases, these enzymes are very dangerous in stingray envenoming related accidents and follow the symptomatology that is characterized by hemorrhage and necrosis in the victim’s affected member 32 .…”

Section: Discussionmentioning

confidence: 82%

“…These enzymes have already been described in stingray venom from Dasyatis pastinaca 32 . Like metalloproteinases, these enzymes are very dangerous in stingray envenoming related accidents and follow the symptomatology that is characterized by hemorrhage and necrosis in the victim’s affected member 32 .…”

Section: Discussionmentioning

confidence: 82%

Venom gland transcriptome analyses of two freshwater stingrays (Myliobatiformes: Potamotrygonidae) from Brazil

Oliveira-Júnior

Fernandes

Cardoso

et al. 2016

Sci Rep

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Stingrays commonly cause human envenoming related accidents in populations of the sea, near rivers and lakes. Transcriptomic profiles have been used to elucidate components of animal venom, since they are capable of providing molecular information on the biology of the animal and could have biomedical applications. In this study, we elucidated the transcriptomic profile of the venom glands from two different freshwater stingray species that are endemic to the Paraná-Paraguay basin in Brazil, Potamotrygon amandae and Potamotrygon falkneri. Using RNA-Seq, we identified species-specific transcripts and overlapping proteins in the venom gland of both species. Among the transcripts related with envenoming, high abundance of hyaluronidases was observed in both species. In addition, we built three-dimensional homology models based on several venom transcripts identified. Our study represents a significant improvement in the information about the venoms employed by these two species and their molecular characteristics. Moreover, the information generated by our group helps in a better understanding of the biology of freshwater cartilaginous fishes and offers clues for the development of clinical treatments for stingray envenoming in Brazil and around the world. Finally, our results might have biomedical implications in developing treatments for complex diseases.

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Enzymatic properties of stingray Dasyatis pastinaca group V, IIA and IB phospholipases A2: A comparative study

Cited by 9 publications

References 35 publications

Transcriptomic Characterization of the South American Freshwater Stingray Potamotrygon motoro Venom Apparatus

Transcriptomic Characterization of the South American Freshwater Stingray Potamotrygon motoro Venom Apparatus

Biochemical, Kinetic and Biological Properties of Group V Phospholipase A2 from Dromedary

Venom gland transcriptome analyses of two freshwater stingrays (Myliobatiformes: Potamotrygonidae) from Brazil

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